ArticleScientific reports2020
Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- Systematic review of accuracy of reporting of Congo red-stained amyloid in 2010-2020 compared with earlier.Annals of medicine · 2022Pooled it
- De Novo Autogenic Engineered Living Functional Materials.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Backbone NMR resonance assignments for the C2 domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2025Article
- Dental plaque biofilm transforms host-derived βBiofilm · 2025Article
- Formative evaluation and structural analysis of non-tuberculosis mycobacterial biofilm using material pieces.Cell surface (Amsterdam, Netherlands) · 2024Article
- Inhibitory effect ofFrontiers in microbiology · 2024Article
- Phytochemical Analysis and Anti-Biofilm Potential That Cause Dental Caries from Black Cumin Seeds (Drug design, development and therapy · 2024Review
- Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2023Article
- Amyloid Fibrils Produced byInternational journal of molecular sciences · 2023Article
- Synchrotron X-ray Studies of the Structural and Functional Hierarchies in Mineralised Human Dental Enamel: A State-of-the-Art Review.Dentistry journal · 2023Review
- Growth with Commensal Streptococci AltersJournal of dental research · 2023Article
- Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Distinct Agents Induce Streptococcus mutans Cells with Altered Biofilm Formation Capacity.Microbiology spectrum · 2022Article
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
- Expression of an Extracellular Protein (SMU.63) Is Regulated by SprV in Streptococcus mutans.Applied and environmental microbiology · 2020Article
- Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions.International journal of molecular sciences · 2020Review
- The Multifaceted Nature of Streptococcal Antigen I/II Proteins in Colonization and Disease Pathogenesis.Frontiers in microbiology · 2020Review
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Streptococcus mutans is an etiologic agent of human dental caries that forms dental plaque biofilms containing functional amyloids. Three amyloidogenic proteins, P1, WapA, and Smu_63c were previously identified. C123 and AgA are naturally occurring amyloid-forming fragments of P1 and WapA, respectively. We determined that four amyloidophilic dyes, ThT, CDy11, BD-oligo, and MK-H4, differentiate C123, AgA, and Smu_63c amyloid from monomers, but non-specific binding to bacterial cells in the absence of amyloid precludes their utility for identifying amyloid in biofilms. Congo red-induced birefringence is a more specific indicator of amyloid formation and differentiates biofilms formed by wild-type S. mutans from a triple ΔP1/WapA/Smu_63c mutant with reduced biofilm forming capabilities. Amyloid accumulation is a late event, appearing in older S. mutans biofilms after 60 hours of growth. Amyloid derived from pure preparations of all three proteins is visualized by electron microscopy as mat-like structures. Typical amyloid fibers become evident following protease digestion to eliminate non-specific aggregates and monomers. Amyloid mats, similar in appearance to those reported in S. mutans biofilm extracellular matrices, are reconstituted by co-incubation of monomers and amyloid fibers. X-ray fiber diffraction of amyloid mats and fibers from all three proteins demonstrate patterns reflective of a cross-β amyloid structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.